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IL9R_MOUSE
ID   IL9R_MOUSE              Reviewed;         468 AA.
AC   Q01114;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Interleukin-9 receptor;
DE            Short=IL-9 receptor;
DE            Short=IL-9R;
DE   AltName: CD_antigen=CD129;
DE   Flags: Precursor;
GN   Name=Il9r;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=T-cell;
RX   PubMed=1376929; DOI=10.1073/pnas.89.12.5690;
RA   Renauld J.-C., Druez C., Kermouni A., Houssiau F., Uyttenhove C.,
RA   van Roost E., van Snick J.;
RT   "Expression cloning of the murine and human interleukin 9 receptor cDNAs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:5690-5694(1992).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH IL9.
RX   PubMed=2145361;
RA   Druez C., Coulie P., Uyttenhove C., Van Snick J.;
RT   "Functional and biochemical characterization of mouse P40/IL-9 receptors.";
RL   J. Immunol. 145:2494-2499(1990).
CC   -!- FUNCTION: Plays an important role in the immune response against
CC       parasites by acting as a receptor of IL9. {ECO:0000269|PubMed:2145361}.
CC   -!- SUBUNIT: Interacts with IL9. {ECO:0000269|PubMed:2145361}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Secreted.
CC   -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC       folding and thereby efficient intracellular transport and cell-surface
CC       receptor binding.
CC   -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC       activation.
CC   -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M84746; AAA37871.1; -; mRNA.
DR   CCDS; CCDS24517.1; -.
DR   PIR; A45268; A45268.
DR   RefSeq; NP_032400.1; NM_008374.2.
DR   AlphaFoldDB; Q01114; -.
DR   SMR; Q01114; -.
DR   STRING; 10090.ENSMUSP00000119557; -.
DR   GlyGen; Q01114; 2 sites.
DR   PhosphoSitePlus; Q01114; -.
DR   PaxDb; Q01114; -.
DR   PRIDE; Q01114; -.
DR   Antibodypedia; 4187; 443 antibodies from 33 providers.
DR   DNASU; 16199; -.
DR   Ensembl; ENSMUST00000145401; ENSMUSP00000118204; ENSMUSG00000020279.
DR   GeneID; 16199; -.
DR   KEGG; mmu:16199; -.
DR   UCSC; uc007iix.2; mouse.
DR   CTD; 3581; -.
DR   MGI; MGI:96564; Il9r.
DR   VEuPathDB; HostDB:ENSMUSG00000020279; -.
DR   eggNOG; ENOG502SB39; Eukaryota.
DR   GeneTree; ENSGT00510000049125; -.
DR   HOGENOM; CLU_614777_0_0_1; -.
DR   InParanoid; Q01114; -.
DR   OMA; CWGVSVP; -.
DR   OrthoDB; 774083at2759; -.
DR   Reactome; R-MMU-8985947; Interleukin-9 signaling.
DR   BioGRID-ORCS; 16199; 2 hits in 74 CRISPR screens.
DR   PRO; PR:Q01114; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q01114; protein.
DR   Bgee; ENSMUSG00000020279; Expressed in spermatocyte and 18 other tissues.
DR   ExpressionAtlas; Q01114; baseline and differential.
DR   Genevisible; Q01114; MM.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR   GO; GO:0019983; F:interleukin-9 binding; IBA:GO_Central.
DR   GO; GO:0004919; F:interleukin-9 receptor activity; IGI:MGI.
DR   GO; GO:0030183; P:B cell differentiation; IGI:MGI.
DR   GO; GO:0042100; P:B cell proliferation; IGI:MGI.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0016064; P:immunoglobulin mediated immune response; IGI:MGI.
DR   GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:MGI.
DR   GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IGI:MGI.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Receptor; Reference proteome;
KW   Secreted; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..468
FT                   /note="Interleukin-9 receptor"
FT                   /id="PRO_0000010912"
FT   TOPO_DOM        38..270
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        292..468
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          148..256
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          407..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           244..248
FT                   /note="WSXWS motif"
FT   MOTIF           301..309
FT                   /note="Box 1 motif"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   468 AA;  52261 MW;  BBE7179FD72E29A5 CRC64;
     MALGRCIAEG WTLERVAVKQ VSWFLIYSWV CSGVCRGVSV PEQGGGGQKA GAFTCLSNSI
     YRIDCHWSAP ELGQESRAWL LFTSNQVTEI KHKCTFWDSM CTLVLPKEEV FLPFDNFTIT
     LHRCIMGQEQ VSLVDSQYLP RRHIKLDPPS DLQSNVSSGR CVLTWGINLA LEPLITSLSY
     ELAFKRQEEA WEARHKDRIV GVTWLILEAV ELNPGSIYEA RLRVQMTLES YEDKTEGEYY
     KSHWSEWSQP VSFPSPQRRQ GLLVPRWQWS ASILVVVPIF LLLTGFVHLL FKLSPRLKRI
     FYQNIPSPEA FFHPLYSVYH GDFQSWTGAR RAGPQARQNG VSTSSAGSES SIWEAVATLT
     YSPACPVQFA CLKWEATAPG FPGLPGSEHV LPAGCLELEG QPSAYLPQED WAPLGSARPP
     PPDSDSGSSD YCMLDCCEEC HLSAFPGHTE SPELTLAQPV ALPVSSRA
 
 
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